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. 2020 Apr 7;29(10):1635–1647. doi: 10.1093/hmg/ddaa059

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© The Author(s) 2020. Published by Oxford University Press.

This is an Open Access article distributed under the terms of the Creative Commons Attribution License (http://creativecommons.org/licenses/by/4.0/), which permits unrestricted reuse, distribution, and reproduction in any medium, provided the original work is properly cited.

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Accumulation of ubiquitinated proteins in the central nervous systems of Ngly1^−/− rats. (A) Ubiquitin-positive inclusions in neurons of Ngly1^−/− rats. Immunohistochemistry of thalamus (TH) and spinal cord (SC) sections from Ngly1^−/− and the WT rats at 5 and 29 weeks of age, stained with an anti-ubiquitin antibody and NeuN, a mature neuron marker. Arrows indicate ubiquitin-positive neurons. Nuclei were stained with DAPI. Scale bar 50 μm. (B, C) Accumulation of Triton-X-100-soluble (B) and insoluble (C) polyubiquitinated proteins in spinal cords of Ngly1^−/− and WT rats. The total protein extracts were separated from the spinal cords of the rats and were separated into Triton-X-100-soluble and Triton-X-100-insoluble fractions and analyzed by immunoblotting using anti-polyubiquitinated antibodies (top) and anti-GAPDH or α-tubulin antibodies (bottom; loading control). Semi-quantitative analyses by densitometry were carried out (B, C). Values represent mean ± SEM (n = 3). Asterisks indicate ^*P < 0.05 and ^*^*P < 0.01.